P20240 · OTE_DROME

Function

function

Inner nuclear membrane protein (PubMed:18410727, PubMed:2186029, PubMed:22751930, PubMed:9199347).
Involved in the attachment of membrane vesicles to chromatin during nuclear assembly, and is probably required for centrosome maturation and cell cycle progression during mitosis (PubMed:22751930, PubMed:9199347).
Essential for differentiation of certain tissues and the maintenance of progenitor cell populations (PubMed:18410727, PubMed:23806619, PubMed:24700158, PubMed:27174470).
Required for the differentiation and maintenance of male and female germline stem cells (GSCs), as well as the maintenance of somatic cells in the GSC niche (PubMed:18410727, PubMed:23806619, PubMed:27174470).
This role is likely to be independent of the BMP (Dpp) pathway that negatively regulates bam transcription during GSC differentiation (PubMed:18410727, PubMed:23806619).
During development, plays essential and redundant functions with the other LEM domain proteins; bocks and MAN1 (PubMed:24700158).
Also has a redundant but important role with bocks during larval development (PubMed:24700158).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcentrosome
Cellular Componentchromosome
Cellular Componentcytoplasm
Cellular Componentendomembrane system
Cellular Componentnuclear envelope lumen
Cellular Componentnuclear inner membrane
Cellular Componentnuclear membrane
Cellular Componentnuclear periphery
Cellular Componentnucleoplasm
Cellular Componentspindle pole
Molecular FunctionDNA-binding transcription factor binding
Molecular Functiontranscription corepressor activity
Biological Processcell division
Biological Processgerm-line stem cell population maintenance
Biological Processgerm-line stem-cell niche homeostasis
Biological Processnegative regulation of DNA-templated transcription
Biological Processnuclear membrane reassembly
Biological Processoogenesis
Biological Processpositive regulation of BMP signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Otefin
  • Alternative names
    • LEM domain-containing protein Otefin

Gene names

    • Name
      Ote
    • ORF names
      CG5581

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    P20240
  • Secondary accessions
    • Q9V8E5

Proteomes

Organism-specific databases

Subcellular Location

Nucleus inner membrane
; Peripheral membrane protein
Nucleus, nucleoplasm
Cytoplasm
Chromosome
Note: Component of the spindle envelope during early mitotic cycles (PubMed:2186029, PubMed:2517292).
Following nuclear envelope breakdown, becomes dispersed in the cytoplasm and concentrated at the spindle poles (PubMed:22751930, PubMed:2517292).
At anaphase (when the nuclear envelope begins to reassemble), locates to the chromosomes accumulating first in areas adjacent to centrosomes and at the peripheral sites of the chromosomes (PubMed:22751930, PubMed:2517292).
At telophase, expressed as a continuous rim around the chromatin and increased expression in the midspindle area (PubMed:22751930).
During cytokinesis, locates to the nuclear periphery with some remaining in the cytoplasm and at the mid-body (PubMed:22751930).
At stage 4 of egg development, expression in the oocyte nuclear envelope is higher than in the nurse nuclear envelope (PubMed:9199347).
Expression in oocyte cytoplasm increases after stages 6 to 7 of egg development (PubMed:9199347).

Keywords

Phenotypes & Variants

Disruption phenotype

No obvious phenotype (PubMed:18410727, PubMed:23806619, PubMed:24700158).
However females are sterile and aging males become prematurely sterile (PubMed:18410727, PubMed:23806619).
Males and females exhibit a range of defects in their germarium that may be age dependent phenotypes (PubMed:18410727, PubMed:23806619, PubMed:27174470).
Most phenotypes result from defects in germline stem cell (GSC) differentiation that often lead to GSC loss (PubMed:23806619, PubMed:27174470).
Also affects somatic cells of the ovarian stem cell niche, with delayed terminal filament formation and cap cell loss (PubMed:27174470).
In 10 day old males, stem cell niches display a decrease in hub cell number but somatic cyst stem cells are unaffected (PubMed:27174470).
No significant decrease in adult survival, however double mutants with either bocks or Man1 do not survive to the adult stage (PubMed:24700158).
Double bocks and Ote mutant larvae have small brains, their imaginal disks are reduced in size or absent, and only 10% of second-instar larvae reach the pupal stage (PubMed:24700158).
In Ote and MAN1 double mutants, pupal survival and larval development is unaffected (PubMed:24700158).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis54Loss of phosphorylation by Cdk1.
Mutagenesis63Prevents phosphorylation and displays an increase in the number of mitotic cells.
Mutagenesis63Phosphomimetic mutant which displays a decrease in the number of mitotic cells.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002061511-424Otefin
Modified residue44Phosphoserine
Modified residue50Phosphoserine
Modified residue54Phosphoserine
Modified residue63Phosphothreonine
Modified residue152Phosphoserine
Modified residue192Phosphoserine
Modified residue198Phosphoserine
Modified residue321Phosphoserine
Modified residue324Phosphothreonine
Modified residue326Phosphoserine
Modified residue358Phosphothreonine
Modified residue378Phosphoserine
Modified residue385Phosphoserine

Post-translational modification

Phosphorylation at Thr-63 by aurA may be required for exit from mitosis (PubMed:22751930).
May be phosphorylated by Cdk1 and Pka-C1 (PubMed:9199347).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in all cell types of the germarium and testis (PubMed:18410727, PubMed:27174470).
Expressed in nurse cells, follicle cells and oocytes (PubMed:9199347).

Developmental stage

Relatively high levels of expression in eggs and 1st instar larvae compared to pupal and adult stages, with weak expression in 2nd instar larvae (at protein level) (PubMed:16439308).
Expressed throughout development in all somatic cells (PubMed:9199347).
Highest levels of expression in embryos and weak expression in larvae and adults (PubMed:2186029, PubMed:9199347).
Expressed throughout development (at protein level) (PubMed:2517292).

Gene expression databases

Interaction

Subunit

Interacts with Med (PubMed:18410727).
Interacts with Lam (PubMed:22751930, PubMed:9632815).
Interacts with aurA, alphaTub84B, gammaTub23C and gammaTub37C (PubMed:22751930).
Interacts with Nemp (PubMed:32923640).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, motif, compositional bias.

TypeIDPosition(s)Description
Domain1-30LEM
Region1-50Required for binding to Med and germline stem cell maintenance
Region42-186Disordered
Motif92-99Nuclear localization signal
Compositional bias99-132Basic and acidic residues
Compositional bias141-159Polar residues
Region259-278Disordered
Compositional bias262-278Polar residues
Region271-400Required for binding to Med
Region400-424Essential for nuclear membrane localization and germline stem cell maintenance
Region406-424Essential for nuclear membrane localization

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    424
  • Mass (Da)
    46,584
  • Last updated
    2004-02-02 v2
  • Checksum
    51E3A83284F7988B
MADVDDFDSLSNAELRAKMLAQGLPNIPVTDSSRKVLVKRLRASIGGQASPAASPKKTNRRETLAPAPGAPSAPAAASTPVDKLDGNKVAPATKARRTITAAEAKEPVRRLPEEAIRRRPDEADRLRSEEPVAARKPTTAPAAQPVQTRRTSTSSGSERKVVEPLRKPETIVEQPASSKRADREENYLKVNSLIVLESDEEEDEQLVQAADLVEQEHAARQKTTKLASSGTTTYEYKSKVVEPPRRQVYEATAAPVLPPSVPSARAQTTSSTRSYDYASNPAPGRYSSFVRTAAQGYVTAEAPPVASYSSSYKRTYANELSDDTDSKEDQYESTFARNLARLRAERIGDRISPYSRRTLASGNAGSGSLGYEPRARRSLRPNDNSVSEAFNRWLNSLEQKYHIKSKLFIVLLVLLLIGVYYIFY

Sequence caution

The sequence CAA35530.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias99-132Basic and acidic residues
Sequence conflict116in Ref. 1; CAA35530
Sequence conflict121in Ref. 1; CAA35530
Sequence conflict128in Ref. 1; CAA35530
Sequence conflict141in Ref. 1; CAA35530
Compositional bias141-159Polar residues
Sequence conflict151in Ref. 1; CAA35530
Sequence conflict186in Ref. 1; CAA35530
Sequence conflict254in Ref. 1; CAA35530
Compositional bias262-278Polar residues
Sequence conflict292in Ref. 1; CAA35530
Sequence conflict344in Ref. 1; CAA35530
Sequence conflict412in Ref. 1; CAA35530

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE013599
EMBL· GenBank· DDBJ
AAF57722.3
EMBL· GenBank· DDBJ
Genomic DNA
AY051940
EMBL· GenBank· DDBJ
AAK93364.1
EMBL· GenBank· DDBJ
mRNA
X17495
EMBL· GenBank· DDBJ
CAA35530.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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